ZN394_HUMAN
ID ZN394_HUMAN Reviewed; 561 AA.
AC Q53GI3; A4D281; Q05DA6; Q6P5X9; Q8TB27; Q9HA37; Q9UD51;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Zinc finger protein 394;
DE AltName: Full=Zinc finger protein with KRAB and SCAN domains 14;
GN Name=ZNF394; Synonyms=ZKSCAN14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15249231; DOI=10.1016/j.bbrc.2004.06.080;
RA Huang C., Wang Y., Li D., Li Y., Luo J., Yuan W., Ou Y., Zhu C., Zhang Y.,
RA Wang Z., Liu M., Wu X.;
RT "Inhibition of transcriptional activities of AP-1 and c-Jun by a new zinc
RT finger protein ZNF394.";
RL Biochem. Biophys. Res. Commun. 320:1298-1305(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, Lung, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 67-143 (ISOFORM 1/2).
RX PubMed=8065901; DOI=10.1093/nar/22.15.2908;
RA Pengue G., Calabro V., Bartoli P.C., Pagliuca A., Lania L.;
RT "Repression of transcriptional activity at a distance by the evolutionarily
RT conserved KRAB domain present in a subfamily of zinc finger proteins.";
RL Nucleic Acids Res. 22:2908-2914(1994).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-203; LYS-228; LYS-254;
RP LYS-282 AND LYS-443, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q53GI3; O95273: CCNDBP1; NbExp=3; IntAct=EBI-10211248, EBI-748961;
CC Q53GI3; P49760: CLK2; NbExp=3; IntAct=EBI-10211248, EBI-750020;
CC Q53GI3; Q15287: RNPS1; NbExp=3; IntAct=EBI-10211248, EBI-395959;
CC Q53GI3; P57086: SCAND1; NbExp=11; IntAct=EBI-10211248, EBI-745846;
CC Q53GI3; Q9UFB7: ZBTB47; NbExp=3; IntAct=EBI-10211248, EBI-7781767;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q53GI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53GI3-3; Sequence=VSP_056547, VSP_056548;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AY642122; AAT67053.1; -; mRNA.
DR EMBL; AK022360; BAB14021.1; -; mRNA.
DR EMBL; AK222948; BAD96668.1; -; mRNA.
DR EMBL; AC073063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236956; EAL23874.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76659.1; -; Genomic_DNA.
DR EMBL; BC017051; AAH17051.1; -; mRNA.
DR EMBL; BC025241; AAH25241.1; -; mRNA.
DR EMBL; BC051847; AAH51847.1; -; mRNA.
DR CCDS; CCDS5666.1; -. [Q53GI3-1]
DR CCDS; CCDS87524.1; -. [Q53GI3-3]
DR RefSeq; NP_001332896.1; NM_001345967.1. [Q53GI3-3]
DR RefSeq; NP_115540.2; NM_032164.3. [Q53GI3-1]
DR AlphaFoldDB; Q53GI3; -.
DR SMR; Q53GI3; -.
DR BioGRID; 123898; 13.
DR IntAct; Q53GI3; 10.
DR STRING; 9606.ENSP00000337363; -.
DR iPTMnet; Q53GI3; -.
DR PhosphoSitePlus; Q53GI3; -.
DR BioMuta; ZNF394; -.
DR DMDM; 81175102; -.
DR jPOST; Q53GI3; -.
DR MassIVE; Q53GI3; -.
DR MaxQB; Q53GI3; -.
DR PaxDb; Q53GI3; -.
DR PeptideAtlas; Q53GI3; -.
DR PRIDE; Q53GI3; -.
DR ProteomicsDB; 62482; -. [Q53GI3-1]
DR ABCD; Q53GI3; 4 sequenced antibodies.
DR Antibodypedia; 16184; 230 antibodies from 25 providers.
DR DNASU; 84124; -.
DR Ensembl; ENST00000337673.7; ENSP00000337363.6; ENSG00000160908.15. [Q53GI3-1]
DR Ensembl; ENST00000426306.2; ENSP00000409565.2; ENSG00000160908.15. [Q53GI3-3]
DR Ensembl; ENST00000651061.1; ENSP00000499131.1; ENSG00000160908.15. [Q53GI3-1]
DR GeneID; 84124; -.
DR KEGG; hsa:84124; -.
DR MANE-Select; ENST00000337673.7; ENSP00000337363.6; NM_032164.4; NP_115540.2.
DR UCSC; uc003uqs.4; human. [Q53GI3-1]
DR CTD; 84124; -.
DR DisGeNET; 84124; -.
DR GeneCards; ZNF394; -.
DR HGNC; HGNC:18832; ZNF394.
DR HPA; ENSG00000160908; Tissue enriched (bone).
DR MIM; 619300; gene.
DR neXtProt; NX_Q53GI3; -.
DR OpenTargets; ENSG00000160908; -.
DR PharmGKB; PA38702; -.
DR VEuPathDB; HostDB:ENSG00000160908; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162347; -.
DR HOGENOM; CLU_002678_49_4_1; -.
DR InParanoid; Q53GI3; -.
DR OMA; EGDSKNN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q53GI3; -.
DR TreeFam; TF337913; -.
DR PathwayCommons; Q53GI3; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q53GI3; -.
DR BioGRID-ORCS; 84124; 14 hits in 1099 CRISPR screens.
DR ChiTaRS; ZNF394; human.
DR GenomeRNAi; 84124; -.
DR Pharos; Q53GI3; Tdark.
DR PRO; PR:Q53GI3; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q53GI3; protein.
DR Bgee; ENSG00000160908; Expressed in mononuclear cell and 186 other tissues.
DR Genevisible; Q53GI3; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..561
FT /note="Zinc finger protein 394"
FT /id="PRO_0000047557"
FT DOMAIN 64..146
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT DOMAIN 155..230
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 358..380
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 386..408
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..436
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..463
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 469..491
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 497..519
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 525..547
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 153..162
FT /note="GMVTFEDTAV -> VWKAEWRTKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056547"
FT VAR_SEQ 163..561
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056548"
FT VARIANT 325
FT /note="T -> M (in dbSNP:rs3735454)"
FT /id="VAR_052816"
FT CONFLICT 3
FT /note="S -> C (in Ref. 2; BAB14021)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="M -> T (in Ref. 3; BAD96668)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="H -> Y (in Ref. 8)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 64256 MW; D92AE5E58DEDAAA5 CRC64;
MNSSLTAQRR GSDAELGPWV MAARSKDAAP SQRDGLLPVK VEEDSPGSWE PNYPAASPDP
ETSRLHFRQL RYQEVAGPEE ALSRLRELCR RWLRPELLSK EQILELLVLE QFLTILPEEL
QAWVREHCPE SGEEAVAVVR ALQRALDGTS SQGMVTFEDT AVSLTWEEWE RLDPARRDFC
RESAQKDSGS TVPPSLESRV ENKELIPMQQ ILEEAEPQGQ LQEAFQGKRP LFSKCGSTHE
DRVEKQSGDP LPLKLENSPE AEGLNSISDV NKNGSIEGED SKNNELQNSA RCSNLVLCQH
IPKAERPTDS EEHGNKCKQS FHMVTWHVLK PHKSDSGDSF HHSSLFETQR QLHEERPYKC
GNCGKSFKQR SDLFRHQRIH TGEKPYGCQE CGKSFSQSAA LTKHQRTHTG EKPYTCLKCG
ERFRQNSHLN RHQSTHSRDK HFKCEECGET CHISNLFRHQ RLHKGERPYK CEECEKSFKQ
RSDLFKHHRI HTGEKPYGCS VCGKRFNQSA TLIKHQRIHT GEKPYKCLEC GERFRQSTHL
IRHQRIHQNK VLSAGRGGSR L
